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Related Concept Videos

Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Protein Diffusion in the Membrane01:24

Protein Diffusion in the Membrane

Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...
Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
Structure of Porins01:21

Structure of Porins

Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel precursors...
Membrane Proteins01:30

Membrane Proteins

Plasma membranes have integral transmembrane proteins involved in facilitated transport. These proteins are collectively referred to as transport proteins, and they function as either channels for the material or as carriers themselves. Channel proteins have hydrophilic domains exposed to the intracellular and extracellular fluids and a hydrophilic channel through their core that provides a hydrated opening for solutes to pass through the membrane layers. Passage through the channel allows...

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Updated: Jun 19, 2026

Membrane-SPINE: A Biochemical Tool to Identify Protein-protein Interactions of Membrane Proteins In Vivo
10:53

Membrane-SPINE: A Biochemical Tool to Identify Protein-protein Interactions of Membrane Proteins In Vivo

Published on: November 7, 2013

Protein-protein interaction in purple membrane.

Maikel C Rheinstädter1, Karin Schmalzl, Kathleen Wood

  • 1Department of Physics and Astronomy, McMaster University, Hamilton, Ontario, L8S 4M1, Canada. rheinstadter@mcmaster.ca

Physical Review Letters
|October 2, 2009
PubMed
Summary

We found evidence of long-range protein interactions in purple membrane using inelastic neutron scattering. This reveals the dynamics and forces within the bacteriorhodopsin protein lattice.

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Last Updated: Jun 19, 2026

Membrane-SPINE: A Biochemical Tool to Identify Protein-protein Interactions of Membrane Proteins In Vivo
10:53

Membrane-SPINE: A Biochemical Tool to Identify Protein-protein Interactions of Membrane Proteins In Vivo

Published on: November 7, 2013

Evaluation of Protein–Protein Interactions using an On-Membrane Digestion Technique
07:07

Evaluation of Protein–Protein Interactions using an On-Membrane Digestion Technique

Published on: July 19, 2019

Protein Membrane Overlay Assay: A Protocol to Test Interaction Between Soluble and Insoluble Proteins in vitro
08:38

Protein Membrane Overlay Assay: A Protocol to Test Interaction Between Soluble and Insoluble Proteins in vitro

Published on: August 14, 2011

Area of Science:

  • Biophysics
  • Structural Biology
  • Materials Science

Background:

  • Purple membrane (PM) is a biological membrane containing bacteriorhodopsin (BR).
  • Understanding protein-protein interactions is crucial for membrane protein function.

Purpose of the Study:

  • To experimentally investigate long-range protein-protein interactions in PM.
  • To quantify interprotein dynamics within the BR lattice.

Main Methods:

  • Inelastic neutron scattering was used to measure acoustic phonon spectra.
  • The 2D protein lattice of bacteriorhodopsin in PM was analyzed.

Main Results:

  • Phonon energies of approximately 1 meV were determined, indicating interprotein dynamics.
  • An effective spring constant (k = 53 N/m) was calculated for interactions between BR trimers.
  • Optical-like excitations at 0.45 meV were observed, attributed to intraprotein dynamics.

Conclusions:

  • Experimental evidence supports long-range interactions between BR trimers in PM.
  • The study quantifies the mechanical properties of the BR protein lattice.